ID PHSG_YEAST Reviewed; 902 AA. AC P06738; D6W4G1; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 4. DT 27-MAR-2024, entry version 212. DE RecName: Full=Glycogen phosphorylase; DE EC=2.4.1.1; GN Name=GPH1; OrderedLocusNames=YPR160W; ORFNames=P9584.1; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3537803; DOI=10.1038/324080a0; RA Hwang P.K., Fletterick R.J.; RT "Convergent and divergent evolution of regulatory sites in eukaryotic RT phosphorylases."; RL Nature 324:80-84(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7871892; DOI=10.1002/yea.320101117; RA Roemer T.D., Fortin N., Bussey H.; RT "DNA sequence analysis of a 10.4 kbp region on the right arm of yeast RT chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two RT novel tRNA genes."; RL Yeast 10:1527-1530(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP PROTEIN SEQUENCE OF 2-10, AND PHOSPHORYLATION AT THR-31. RX PubMed=1613787; DOI=10.1016/0022-2836(92)90102-p; RA Rath V.L., Hwang P.K., Fletterick R.J.; RT "Purification and crystallization of glycogen phosphorylase from RT Saccharomyces cerevisiae."; RL J. Mol. Biol. 225:1027-1034(1992). RN [6] RP PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, AND RP PYRIDOXAL PHOSPHATE AT LYS-751. RX PubMed=1092346; DOI=10.1021/bi00680a031; RA Lerch K., Fischer E.H.; RT "Amino acid sequence of two functional sites in yeast glycogen RT phosphorylase."; RL Biochemistry 14:2009-2014(1975). RN [7] RP SUBUNIT. RX PubMed=6354094; DOI=10.1016/0003-9861(83)90078-4; RA Becker J.U., Wingender-Drissen R., Schiltz E.; RT "Purification and properties of phosphorylase from baker's yeast."; RL Arch. Biochem. Biophys. 225:667-678(1983). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-333, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-333, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=24146988; DOI=10.1371/journal.pone.0077380; RA Gsell M., Mascher G., Schuiki I., Ploier B., Hrastnik C., Daum G.; RT "Transcriptional response to deletion of the phosphatidylserine RT decarboxylase Psd1p in the yeast Saccharomyces cerevisiae."; RL PLoS ONE 8:e77380-e77380(2013). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-901. RX PubMed=8703213; DOI=10.1126/science.273.5281.1539; RA Lin K., Rath V.L., Dai S.C., Fletterick R.J., Hwang P.K.; RT "A protein phosphorylation switch at the conserved allosteric site in GP."; RL Science 273:1539-1542(1996). CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in CC carbohydrate metabolism. Enzymes from different sources differ in their CC regulatory mechanisms and in their natural substrates. However, all CC known phosphorylases share catalytic and structural properties. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-31. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6354094}. CC -!- INTERACTION: CC P06738; P33203: PRP40; NbExp=2; IntAct=EBI-13389, EBI-701; CC P06738; P39940: RSP5; NbExp=2; IntAct=EBI-13389, EBI-16219; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24146988}. CC -!- DISRUPTION PHENOTYPE: Decreases cellular phosphatidylcholine levels CC (PubMed:24146988). Growth on non-fermentable carbon sources is severely CC decreased (lactate or glycerol) (PubMed:24146988). Sensitive to sodium CC dodecyl sulfate, and sorbitol (PubMed:24146988). CC {ECO:0000269|PubMed:24146988}. CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA28273.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04604; CAA28273.1; ALT_INIT; Genomic_DNA. DR EMBL; L33835; AAB59313.1; -; Genomic_DNA. DR EMBL; U28371; AAB68057.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11577.1; -; Genomic_DNA. DR PIR; S61144; S61144. DR RefSeq; NP_015486.1; NM_001184257.1. DR PDB; 1YGP; X-ray; 2.80 A; A/B=24-902. DR PDBsum; 1YGP; -. DR AlphaFoldDB; P06738; -. DR SMR; P06738; -. DR BioGRID; 36333; 299. DR DIP; DIP-2648N; -. DR IntAct; P06738; 26. DR MINT; P06738; -. DR STRING; 4932.YPR160W; -. DR CAZy; GT35; Glycosyltransferase Family 35. DR iPTMnet; P06738; -. DR MaxQB; P06738; -. DR PaxDb; 4932-YPR160W; -. DR PeptideAtlas; P06738; -. DR EnsemblFungi; YPR160W_mRNA; YPR160W; YPR160W. DR GeneID; 856289; -. DR KEGG; sce:YPR160W; -. DR AGR; SGD:S000006364; -. DR SGD; S000006364; GPH1. DR VEuPathDB; FungiDB:YPR160W; -. DR eggNOG; KOG2099; Eukaryota. DR GeneTree; ENSGT00950000183148; -. DR HOGENOM; CLU_010198_1_0_1; -. DR InParanoid; P06738; -. DR OMA; WLKQANP; -. DR OrthoDB; 5473321at2759; -. DR BioCyc; MetaCyc:YPR160W-MONOMER; -. DR BioCyc; YEAST:YPR160W-MONOMER; -. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis). DR BioGRID-ORCS; 856289; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P06738; -. DR PRO; PR:P06738; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P06738; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:SGD. DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0005980; P:glycogen catabolic process; IMP:SGD. DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR011833; Glycg_phsphrylas. DR InterPro; IPR000811; Glyco_trans_35. DR InterPro; IPR035090; Pyridoxal_P_attach_site. DR NCBIfam; TIGR02093; P_ylase; 1. DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1. DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1. DR Pfam; PF00343; Phosphorylase; 1. DR PIRSF; PIRSF000460; Pprylas_GlgP; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00102; PHOSPHORYLASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cytoplasm; KW Direct protein sequencing; Glycogen metabolism; Glycosyltransferase; KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1613787" FT CHAIN 2..902 FT /note="Glycogen phosphorylase" FT /id="PRO_0000188545" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 31 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:1092346, FT ECO:0000269|PubMed:1613787, ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 751 FT /note="N6-(pyridoxal phosphate)lysine" FT CONFLICT 167..168 FT /note="DL -> EG (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="A -> P (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT CONFLICT 440..441 FT /note="VG -> RR (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT CONFLICT 508 FT /note="A -> V (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="V -> I (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT CONFLICT 578 FT /note="G -> E (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT CONFLICT 876 FT /note="V -> L (in Ref. 1; CAA28273 and 2; AAB59313)" FT /evidence="ECO:0000305" FT HELIX 35..44 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 47..55 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 64..76 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 88..117 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 158..168 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 172..176 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 188..202 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 235..238 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 244..256 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 277..290 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 297..308 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 313..317 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 321..324 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 326..336 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 345..372 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 380..383 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 384..391 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 395..406 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 412..422 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 423..427 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 440..446 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 448..468 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 474..479 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 481..483 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 486..488 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 493..500 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 501..508 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 509..517 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 518..520 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 521..527 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 529..531 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 532..534 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 541..544 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 545..548 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 550..559 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 566..568 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 571..582 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 585..607 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 608..611 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 620..622 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 624..630 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 634..636 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 638..657 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 662..668 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 672..677 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 685..701 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 705..707 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 710..716 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 721..727 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 728..730 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 732..736 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 747..753 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 754..756 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 758..763 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 766..774 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 776..778 FT /evidence="ECO:0007829|PDB:1YGP" FT STRAND 779..783 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 786..798 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 805..813 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 824..827 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 828..836 FT /evidence="ECO:0007829|PDB:1YGP" FT TURN 838..841 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 843..863 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 865..879 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 880..882 FT /evidence="ECO:0007829|PDB:1YGP" FT HELIX 884..894 FT /evidence="ECO:0007829|PDB:1YGP" SQ SEQUENCE 902 AA; 103275 MW; F5B6098D69ABAE43 CRC64; MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR ALWNKHQVKK FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR DNLVIDWNKT QQKFTTRDPK RVYYLSLEFL MGRALDNALI NMKIEDPEDP AASKGKPREM IKGALDDLGF KLEDVLDQEP DAGLGNGGLG RLAACFVDSM ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN PWEIERNEVQ IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL RLKQQYFWCA ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL QRVLVDLEKL DWHEAWDIVT KTFAYTNHTV MQEALEKWPV GLFGHLLPRH LEIIYDINWF FLQDVAKKFP KDVDLLSRIS IIEENSPERQ IRMAFLAIVG SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT PRRWLKQANP SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL AMKNMLKNGA SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI VNNDESIEHL LKVVFVADYN VSKAEIIIPA SDLSEHISTA GTEASGTSNM KFVMNGGLII GTVDGANVEI TREIGEDNVF LFGNLSENVE ELRYNHQYHP QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY YLVSDDFESY LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP VT //